ID A0A021VT11_9CELL Unreviewed; 466 AA.
AC A0A021VT11;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N866_13320 {ECO:0000313|EMBL:EYR64291.1};
OS Actinotalea ferrariae CF5-4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Actinotalea.
OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR64291.1, ECO:0000313|Proteomes:UP000019753};
RN [1] {ECO:0000313|EMBL:EYR64291.1, ECO:0000313|Proteomes:UP000019753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR64291.1,
RC ECO:0000313|Proteomes:UP000019753};
RA Chen F., Li Y., Wang G.;
RT "Actinotalea ferrariae CF5-4.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYR64291.1}.
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DR EMBL; AXCW01000038; EYR64291.1; -; Genomic_DNA.
DR RefSeq; WP_052022432.1; NZ_AXCW01000038.1.
DR AlphaFoldDB; A0A021VT11; -.
DR OrthoDB; 3246809at2; -.
DR Proteomes; UP000019753; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000019753}.
SQ SEQUENCE 466 AA; 51732 MW; 5C050DAA88E1B2C2 CRC64;
MTETMGTTST TPAGTDRQEA ARNHLWGHMT RQSTWEKGHV PVIVRGRGHH IWDAEGRRYI
DGLSGLFVVQ AGHGRAELAE RARQQAEELA FFPLWSYAHP QAIDLAERLA HHAPGDLNRI
FFTTGGGEAV ETAWKLAKQY WKLMGQPTKY KVISRAVAYH GTPQGALAIT GLPGMKAPFE
PLVPGAHKVP NTNIYRAPVE LRDDPKAFGR WAADRIEEAI LFEGPETVAA VFLEPVQNSG
GCFPPPPGYF ERVREICDQY DVLLVSDEVI CAFGRVGEIF ACNEYGYVPD MITCAKGMTS
GYSPIGATVV SDRIFEPFRT GTTTFYHGYT FGGHPVSAAV AMANLDIFEQ ERLTQRVHEN
GPVFRRTLEK LLDLPIVGDV RGDGYFYGIE LVKDQATRET FDDDESERLL RGFLSHALLD
AGLYCRADDR GDPVIQLAPP LTIGPAEFDE IEQILRDVLS RAWAQL
//
